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Updated: May 5, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
Published on: January 20, 2023
Dimerization of a heat shock protein 90 inhibitor enhances inhibitory activity
Hendra Wahyudi1, Yao Wang, Shelli R McAlpine
1Department of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia. s.mcalpine@UNSW.edu.au.
Abstract:
Heat shock protein 90 (hsp90) accounts for 1-2% of the total proteins in normal cells and it functions as a dimer. Hsp90 behaves as a molecular chaperone that folds, assembles, and stabilizes client proteins. We have developed a novel hsp90 inhibitor, and herein we describe the synthesis and biological activity of the dimerized variant of this inhibitor. Tethering a monomer inhibitor together produced a dimerized compound that more effectively inhibits hsp90 over the monomer.
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